title: Crystallization of the Staphylococcus aureus MazF mRNA interferase.
abstract: mazEF modules encode toxin-antitoxin pairs that are involved in the bacterial stress response through controlled and specific degradation of mRNA. Staphylococcus aureus MazF and MazE constitute a unique toxin-antitoxin module under regulation of the sigB operon. A MazF-type mRNA interferase is combined with an antitoxin of unknown fold. Crystals of S. aureus MazF (SaMazF) were grown in space group P2(1)2(1)2(1). The crystals diffracted to 2.1 Å resolution and are likely to contain two SaMazF dimers in the asymmetric unit.
authors.affiliation: Structural Biology Brussels, Department of Molecular and Cellular Interactions, Vrije Universiteit Brussel, Pleinlaan 2, B-1050 Brussel, Belgium.
authors.forename: Valentina
authors.initials: V
authors.lastname: Zorzini
authors.forename: Sarah
authors.initials: S
authors.lastname: Haesaerts
authors.forename: Niles P
authors.initials: NP
authors.lastname: Donegan
authors.forename: Zhibiao
authors.initials: Z
authors.lastname: Fu
authors.forename: Ambrose L
authors.initials: AL
authors.lastname: Cheung
authors.forename: Nico A J
authors.initials: NA
authors.lastname: van Nuland
authors.forename: Remy
authors.initials: R
authors.lastname: Loris
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins / Q000737:chemistry*; D004722:Endoribonucleases / Q000737:chemistry*; D008969:Molecular Sequence Data; D012333:RNA, Messenger / Q000378:metabolism*; D013211:Staphylococcus aureus / Q000201:enzymology*
chemical_list: D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D012333:RNA, Messenger; D004722:Endoribonucleases